(data stored in SCRATCH zone)

SWISSPROT: Q5LVR6_RUEPO

ID   Q5LVR6_RUEPO            Unreviewed;       465 AA.
AC   Q5LVR6;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   SubName: Full=Oxidoreductase, FAD-binding protein {ECO:0000313|EMBL:AAV93942.1};
GN   OrderedLocusNames=SPO0634 {ECO:0000313|EMBL:AAV93942.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93942.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93942.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93942.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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DR   EMBL; CP000031; AAV93942.1; -; Genomic_DNA.
DR   RefSeq; WP_011046385.1; NC_003911.12.
DR   STRING; 246200.SPO0634; -.
DR   EnsemblBacteria; AAV93942; AAV93942; SPO0634.
DR   KEGG; sil:SPO0634; -.
DR   eggNOG; ENOG4105CQB; Bacteria.
DR   eggNOG; COG0277; LUCA.
DR   HOGENOM; HOG000230995; -.
DR   KO; K00102; -.
DR   OMA; RHDAYWS; -.
DR   OrthoDB; 1188552at2; -.
DR   BioCyc; RPOM246200:G1G48-645-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.10.45.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
DR   PRODOM; Q5LVR6.
DR   SWISS-2DPAGE; Q5LVR6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   DOMAIN       47    224       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   465 AA;  49579 MW;  C95BB8E8ADF84119 CRC64;
     MAQITALPRN ETGIETVIGI LRQRFGDRLQ TGQAIREQHG HTTTWIQNQP PDAVVFPTST
     AEVSEIVKTC AEHKVAVIPF GTGTSLEGHV NAPAGGISVD LMQMNNILAV HAGDLDCVVQ
     PGVTREQLNT HLRDQGLFFP IDPGANASLG GMASTRASGT NAVRYGTMKD NVLALEVVMP
     DGEVIRTAQR AKKTSAGYDL TRLMIGAEGT LGIITEITLK LQGIPEAISA ARCSFPTVDA
     ACQAVMTTIQ FGIPVARMEL LDVIAVQAVN AYSKLDLPET PLLLLEFHGS EAGVAEQAEL
     FGSIAEENEG SGFAWTTSTE ERNRLWKARH EFYWASLQLR PGCSALATDV CVPISRLAEC
     VNAATAKAEE LGLFAPLVGH VGDGNFHISP LIDKDDPAEV ATTEAFTAWL AELAISMDGT
     CTGEHGIGQG KRAYLSRELG QTPRYMAAIK AALDPLGIMN PGKIL
//

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